COVID-19: The Emprins Morning Prayer & ROCK

Recent research indicates that the gene CD147, otherwise known as Emprin, is a Target for COVID-19 Treatment.

CD147, a receptor on host cells, also known as Basigin and Emprin, is a novel route for the SARS-CoV-2 invasion. Thus, compounds that interfere in the spike protein/CD147 interaction or CD147 expression may inhibit viral invasion and dissemination among other cells, including in progenitor/stem cells.[1]

CD147 is a highly glycosylated transmembrane protein of the immunoglobulin superfamily that acts as the main upstream stimulator of matrix metalloproteinases (MMPs).

In another study, we see that “SARS-CoV-2 invades host cells via a novel route: CD147-spike protein.[2]

And again another study states “BREAKING! New Coronavirus Research Shows That The SARS-CoV-2 Coronavirus Has A Fourth Route Of Attacking Human Host Cells Making It A Real Super Virus.”[3]

Let’s break down this EMPRIN (CD147 gene)[4] and do our due DNA Diligence!

First, the BSG Gene has aliases of:

· Ok Blood Group

· Basigin



· SLC7A11

· CD147

· OK

First, EMPRIN is also known as Aspirin[5].

Aspirin is used to reduce fever and relieve mild to moderate pain from conditions such as muscle aches, toothaches, common cold, and headaches. It may also be used to reduce pain and swelling in conditions such as arthritis. Aspirin is known as a salicylate and a nonsteroidal anti-inflammatory drug (NSAID). It works by blocking a certain natural substance in your body to reduce pain and swelling.

Protective Effect of Aspirin on COVID-19 Patients[6]

Study Description

Brief Summary:

“COVID-19 has a high infection rate and mortality, and serious complications such as heart injury cannot be ignored. Cardiac dysfunction occurred in COVID-19 patients, but the law and mechanism of cardiac dysfunction remain unclear. The occurrence of progressive inflammatory factor storm and coagulation dysfunction in severe and fatal cases of NCP points out a new direction for reducing the incidence of severe and critically ill patients, shortening the length of duration in severe and critically ill patients and reducing the incidence of complications of cardiovascular diseases.

Aspirin has the triple effects of inhibiting virus replication, anticoagulant, and anti-inflammatory, but it has not received attention in the treatment and prevention of NCP. Although Aspirin is not commonly used in the guidelines for the treatment of NCP, it was widely used in the treatment and prevention of a variety of human diseases after its first synthesis in 1898. Subsequently, aspirin has been confirmed to have an antiviral effect on multiple levels. Moreover, one study has confirmed that aspirin can inhibit virus replication by inhibiting prostaglandin E2 (PGE2) in macrophages and upregulation of type I interferon production. Subsequently, pharmacological studies have found that aspirin as an anti-inflammatory and analgesic drug by inhibiting cox-oxidase (COX). Under certain conditions, the platelet is the main contributor of the innate immune response, studies have found that in the lung injury model in dynamic neutrophil and platelet aggregation.

In summary, the early use of aspirin in COVID-19 patients, which has the effects of inhibiting virus replication, anti-platelet aggregation, anti-inflammatory, and anti-lung injury, is expected to reduce the incidence of severe and critical patients, shorten the length of hospital duration and reduce the incidence of cardiovascular complications.”

Is it safe to take aspirin to treat coronavirus symptoms?[7]


For adults, it’s safe to take aspirin for pain or fever from COVID-19. Due to initial concern that anti-inflammatory drugs like and may worsen coronavirus symptoms, the World Health Organization initially recommended against the use of these anti-inflammatory drugs. However, they reversed that recommendation several days later and no longer recommend against ibuprofen or other anti-inflammatory drugs, including aspirin. Children and teenagers should not take aspirin due to the risk of it causing a life-threatening condition called Reye’s syndrome.

Willow Bark (Salix alba)

Willow bark has been used for centuries as a treatment for pain, headache, and inflammatory conditions such as bursitis and tendinitis. The bark of white willow contains salicin, the chemical that was used to develop aspirin[8].

For centuries, herbal medicines have been traditionally utilized for the treatment of various ailments, including viral diseases. The discoveries of effective Western medicines, such as aspirin, which can be obtained from white Willow bark, have increased the interest for more elaborate research on herbal medicines and paved the way toward the acceptance of the efficacy of using standardized herbal preparations[9].


EMPRIN gene is a plasma membrane protein that is important in spermatogenesis, embryo implantation, neural network formation, and tumor progression. It is also a member of the immunoglobulin superfamily, ubiquitously expressed in various tissues[10].

The EMPRIN (CD147 gene) is a receptor for oligomannosidic glycans.

Oligomannosidic glycans require Mannose, N-Acetyl Glucosamine (NAG), and Fucose (Bladderwrack).[11]

The Function of Oligomannosidic N-Glycans

Oligomannosidic N-glycans are implicated in the folding of nascent polypeptides and play an important role during ER-quality control processes and ERAD of misfolded or incompletely assembled glycoproteins[12].

Oligomannosidic glycans are also essential for secretion of human diamine oxidase (DAO) required for histamine catabolism (breakdown)[13].

Diamine oxidase, also known as histaminase, is an enzyme involved in the metabolism, oxidation, and inactivation of histamine and other polyamines such as putrescine or spermidine.

In other words, if Mannose and N-Acetyl Glucosamine are not present, DOA does not function correctly, which goes on to manifest with symptoms of allergies or histamine intolerance.

Native HIV Glycans Are Oligomannose[14], and there is an uncanny similarity of unique inserts in the 2019-nCoV spike protein to HIV-1 gp120 and Gag[15].

Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens.

Again, your systems biology needs Mannose, N-Acetyl Glucosamine, and Fucose (Bladderwrack) to deal with HIV-1 and 2019-nCoV spike proteins.

These viruses contain a shield called a glycan shield that allows them to evade host system immune surveillance.

This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterized across other viral glycoproteins, such as HIV-1 envelope protein (Env), influenza hemagglutinin (HA) and Lassa virus glycoprotein complex (LASV GPC)[16].

Glycosylation is a ubiquitous post-translational modification responsible for a multitude of crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to glycosylate their own proteins during replication.

Viral envelope proteins from a variety of human pathogens including HIV-1, influenza virus, Lassa virus, SARS, Zika virus, dengue virus, and Ebola virus have evolved to be extensively glycosylated. These host-cell derived glycans facilitate diverse structural and functional roles during the viral life-cycle, ranging from immune evasion by glycan shielding to enhancement of immune cell infection[17].

· Enveloped viruses often hijack host-cell glycosylation pathways.

· Viral glycans have multifaceted influences on pathobiology.

· Glycans have intrinsic functionalities but can also be influenced by immune selection.

· Viral glycobiology is emerging as an important parameter during vaccine design.

Viral glycosylation has been investigated in the context of a number of envelope glycoproteins, including the envelope glycoprotein (Env) of human immunodeficiency virus-1 (HIV-1), hemagglutinin glycoprotein (HA) of influenza virus, coronavirus glycoprotein spike (S), glycoprotein (GP) of Ebola virus, glycoprotein complex (GPC) of Lassa virus, and envelope (E) glycoprotein of dengue, Zika, and other flaviviruses.

Again, viral proteins are glycosylated by the host-cell as viruses are able to hijack cellular glycosylation.

The most important factors in relation to the “Glycan key” are Mannose, N-Acetyl Glucosamine, and Fucose (Bladderwrack).

Glycosylation in viral release

Some viruses exploit the glycosylation pathways not only to modify their own proteins but also utilize host glycans as receptors and attachment factors, however, these same interactions can impede viral budding from the infected cell.

Consequently, such viruses have evolved carbohydrate-cleaving enzymes to facilitate efficient viral budding and release. The most notable example is the ability of neuraminidases of influenza viruses to cleave sialic acid residues on the host cell surface to negate the ability of hemagglutinins (HA) to bind the host-cell receptor sugars.

Therefore, in order to attenuate for this, the use of viral neuraminidase inhibitors may be deployed.

Chinese skullcap is one such compound.

Baicalein (Skullcap), Ethyl Acetate, and Chloroform Extracts of Scutellaria baicalensis Inhibit the Neuraminidase Activity of Pandemic 2009 H1N1 and Seasonal Influenza A Viruses[18]

Licorice root is another such compound..

Neuraminidase (NA), a key enzyme in viral replication, is the first-line drug target to combat influenza. On the basis of a shape-focused virtual screening, the roots of Glycyrrhiza glabra (Licorice) were identified as plant species with an accumulation of constituents that show 3D similarities to known influenza NA inhibitors (NAIs)[19].

All together now we see that the synergy of Mannose, N-Acetyl Glucosamine, Fucose (Bladderwrack), Skullcap, and Licorice work of a wide array of stealth pathogens, including viruses!

Matrix Metalloproteinases (MMPs)

As previously discussed, CD147 acts as the main upstream stimulator of matrix metalloproteinases (MMPs).

Matrix metallopeptidases (MMPs), also known as matrix metalloproteinases or matrixins, are metalloproteinases that are calcium-dependent zinc-containing endopeptidases[20].

Collectively, these enzymes are capable of degrading all kinds of extracellular matrix proteins, but also can process a number of bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands (such as the FAS ligand), and chemokine/cytokine inactivation.

The Role of Metalloproteinases in Corona Virus Infection[21]

The persistence of viral RNA and inflammatory cells within the CNS is associated with the development of ongoing demyelination. Matrix metalloproteinases (MMPs) are a family of proteases involved in the degradation of the extracellular matrix (ECM).

During inflammatory responses, MMPs are thought to play a significant role in breaking down the basement membrane surrounding blood vessels as well as parenchymal ECM thereby facilitating leukocyte infiltration.

MMPs have also been associated with the activation of chemokines and perhaps more significantly the degradation of myelin proteins and generation of autoantigens.

A recent examination of MMP expression during MHV infection suggests that MMP-3, -9, and -12 are involved in the inflammatory response. The proinflammatory effects of these MMPs are likely tempered by the induction of tissue inhibiter of metalloproteinase-1 expression.

MMPs are inhibited by specific endogenous tissue inhibitor of metalloproteinases (TIMPs), which comprise a family of four protease inhibitors: TIMP-1, TIMP-2, TIMP-3, and TIMP-4.

Zinc and Calcium both are vital for the proper function of MMPs.

MMPs play crucial roles in numerous pathophysiological conditions, including cancer, cardiovascular disease, autoimmune diseases, skin aging, inflammation, etc.

Nutraceuticals which include Genistein (Nattokinase), Myricetin (Sea buckthorn), Resveratrol, Betulinic acid (Prunella vulgaris), Oleanolic acid (Prunella vulgaris), and Glycyrrhetinic acid (Licorice), target specific MMPs[22].

In addition, according to a recent study[23] done on natural anti-viral compounds, we see that CORONAVIRUS compounds include:

“Natural inhibitors against the SARS-CoV enzymes, such as the nsP13 helicase and 3CL protease, have been identified as well and include myricetin, scutellarein”

These would be Skullcap and Sea buckthorn. Sea buckthorn contains the bioactive molecule myricetin[24].

In fact, a recent study is drawing the attention of the medical community, claiming that sea buckthorn berry’s lactic acid bacteria can contain the spread of the new coronavirus by inhibiting the activation of its energy source, purine.[25]

Fucoidan, or Bladderwrack, also inhibits Matrix Metalloproteinases in association with CD147[26].

Degradation of Myelin

EMPRIN also interacts with MAG (Myelin Associated Glycoprotein/Siglec-4).

MAG is a critical protein in the formation and maintenance of myelin sheaths[27].

MAG is believed to be involved in myelination during nerve regeneration in the PNS and is vital for the long-term survival of the myelinated axons following myelinogenesis.

In the CNS MAG is one of three main myelin-associated inhibitors of axonal regeneration after injury, making it an important protein for future research on neurogenesis in the CNS.

Malfunctions to the MAG gene are implicated in demyelination diseases such as multiple sclerosis.

During more recent viral outbreaks, such as SARS-CoV-1 in 2003, H1N1 in 2009, and MERS-CoV in 2012, there were subsequent reports of higher rates of narcolepsy, seizures, encephalitis (brain inflammation), Guillain-Barre syndrome and other neuromuscular and demyelinating conditions[28].

COVID-19 has been linked to Guillain-Barré Syndrome, an autoimmune disease that causes abnormal sensation and weakness due to delays in sending signals through the nerves[29].

MAG is a member of the immunoglobulin superfamily. It is thought to be involved in the process of myelination. It is a lectin that binds to sialylated glycoconjugates and mediates certain myelin-neuron cell-cell interactions[30].

Sialylated glycoconjugates have everything to do with neuraminidases, sialic acid, and hemagglutinins (HA), as previously discussed.

Sialic acid, and subsequently neuraminidases, may be attenuated for through viral neuraminidase inhibitors such as Skullcap and Licorice.

Overexpression of sialic acid on surfaces creates a negative charge on cell membranes. This creates repulsion between cells (cell opposition) and helps, for example, late-stage cancer cells enter the blood stream[31].

Sialic acid helps pathogens evade the innate immune response of the host.

Sialic acid can "hide" mannose antigens on the surface of host cells or bacteria from mannose-binding lectin. This prevents the activation of complement.


Many viruses such as some adenoviruses (Adenoviridae), rotaviruses (Reoviridae) and influenza viruses (Orthomyxoviridae) can use host-sialylated structures for binding to their target host cell. Sialic acids provide a good target for these viruses since they are highly conserved and are abundant in large numbers in virtually all cells.

Unsurprisingly, sialic acids also play an important role in several human viral infections. The influenza viruses have hemagglutinin activity (HA) glycoproteins on their surfaces that bind to sialic acids found on the surface of human erythrocytes and on the cell membranes of the upper respiratory tract.

This is the basis of hemagglutination when viruses are mixed with blood cells and entry of the virus into cells of the upper respiratory tract. Widely used anti-influenza drugs (oseltamivir and zanamivir) are sialic acid analogs that interfere with the release of newly generated viruses from infected cells by inhibiting the viral enzyme neuraminidase.

Again, this is what Skullcap and Licorice accomplish as they are natural viral neuraminidase inhibitors.

Also, sialylated molecules of human milk can be recognized and bound by sialic acid-dependent pathogens and inhibit their adhesion to the epithelial cells of newborns and infants[32].

Morning Prayers

The EMPRIN gene (CD147), through its interactive DNA string network[33], is regulated by MATINS (MYH9 Gene).

Myosin Heavy Chain 9 (MYH9 Gene) has the alias of MATINS[34].

The etymology of MATINS means Morning prayers[35].

From Late Latin matutinas (nominative matutinæ) "morning prayers," originally matutinas vigilias "morning watches," from Latin matutinus "of or in the morning," associated with Matuta, Roman dawn goddess (see manana)[36].

Mater Matuta[37]

Mother goddess seated in a wicker chair and nursing an infant, sometimes identified as Mater Matuta.

Commonly called Mater Matuta, is usually considered as the goddess of the dawn of morning.

The MATINS gene

The MATINS gene (myosin heavy chain 9) plays a role in cell movement (cell motility); maintenance of cell shape; and cytokinesis, which is the step in cell division when the fluid surrounding the nucleus (the cytoplasm) divides to form two separate cells. While some cells use more than one type of myosin II, certain blood cells such as platelets and white blood cells (leukocytes) use only myosin IIA[38].

Myosins are a large family of motor proteins that share the common features of ATP hydrolysis (ATPase enzyme activity), actin binding and potential for kinetic energy transduction.

Human Phenotype Ontology for MYH9 Gene[39]:

· Abnormal thrombosis - Abnormal blood clot

· Bruising susceptibility

· Congenital thrombocytopenia - severely low number of megakaryocytes, a type of bone marrow cell that makes platelets that are important for clotting and preventing bleeding

· Elevated hepatic transaminase - Elevated liver enzymes

· Epistaxis - Bloody nose

· Giant platelets

· High-frequency hearing impairment - Hearing loss

· Others

Compounds for MYH9 Gene[40]:

· Artemisinin


Rho kinase (ROCK) inhibitors also regulate myosin II ATPases such as MATINS gene (myosin heavy chain 9)[41].

MAG (Myelin Associated Glycoprotein/Siglec-4), as previously mentioned also communicates with Rho kinase (ROCK)[42].

This study speaks about the restoring capacity of ROCK inhibition…ROCKing regeneration: Rho kinase inhibition as a molecular target for neurorestoration[43]

ROCK can be regulated by lipids, in particular arachidonic acid[44].

Arachidonic acid is a polyunsaturated fatty acid present in the phospholipids (especially phosphatidylethanolamine, phosphatidylcholine, and phosphatidylinositides) of membranes of the body's cells, and is abundant in the brain, muscles, and liver[45].

Arachidonic acid may also be found in Sea buckthorn[46].

Study: Effects of sea buckthorn berries on infections and inflammation: a double-blind, randomized, placebo-controlled trial[47]

Arachidonic acid is metabolized to both pro-inflammatory and anti-inflammatory eicosanoids during and after the inflammatory response, respectively.

Arachidonic acid is also metabolized to inflammatory and anti-inflammatory eicosanoids during and after physical activity to promote growth. However, chronic inflammation from exogenous toxins and excessive exercise should not be confused with acute inflammation from exercise and sufficient rest that is required by the inflammatory response to promote the repair and growth of the micro-tears of tissues.

However, the evidence is mixed. Some studies giving between 840 mg and 2,000 mg per day to healthy individuals for up to 50 days have shown no increases in inflammation or related metabolic activities. However, others show that increased arachidonic acid levels are actually associated with reduced pro-inflammatory IL-6 and IL-1 levels and increased anti-inflammatory tumor necrosis factor-beta. This may result in a reduction in systemic inflammation.

ROCK Inhibitors

Licorice and Baicalein (Skullcap) showed potential therapeutics for pulmonary hypertension in relation to ROCK inhibition[48].

These are the same EXACT two compounds that show viral neuraminidase inhibition, as stated above. [EMPHASIS ADDED]

Quick Recap

So basically, ROCK inhibition impacts the MAG gene associated with myelin and the Morning Prayer gene (The MATINS gene/MYH9), which ultimately impacts the function of EMPRIN/CD147, and subsequently COVID19.

Study: Acute lung injury: The therapeutic role of Rho kinase inhibitors[49]

Upregulation of the RhoA/ROCK signaling pathway causes an increase of inflammation, immune cell migration, apoptosis, coagulation, contraction, and cell adhesion in pulmonary endothelial cells. These effects are involved in endothelium barrier dysfunction and edema, hallmarks of ALI (Acute lung injury). These effects were significantly reversed by Rho kinase inhibitors. Rho kinase inhibition offers a promising approach in ALI [ARDS] treatment.”

Study: Could pharmacological curtailment of the RhoA/Rho-kinase pathway reverse the endothelial barrier dysfunction associated with Ebola virus infection?[50]

“Activation of the RhoA/Rho-kinase (ROCK) pathway induces endothelial barrier dysfunction and increased vascular permeability, which is a hallmark of various life-threatening vascular pathologies. Therapeutic approaches aimed at inhibiting the RhoA/ROCK pathway have proven effective in the attenuation of vascular leakage observed in animal models of endotoxin-induced lung injury/sepsis, edema, autoimmune disorders, and stroke. These findings suggest that treatments targeting the ROCK pathway might be of benefit in the management of the Ebola virus disease (EVD), which is characterized by severe vascular leak, likely involving pro-inflammatory cytokines, such as tumor necrosis factor-alpha, released from virus-infected macrophages. In this paper, we review evidence from in vivo and in vitro models of vascular leakage, suggesting that the RhoA/ROCK pathway is an important therapeutic target for the reversal of the vascular permeability defects associated with EVD.”

Rho/ROCK Inhibitors - Rho-associated, coiled-coil containing protein kinase 1 (ROCK1) is an important regulator of focal adhesion[51]. ROCKs have been regarded as promising targets for the treatment of cardiovascular diseases, neurological diseases, and cancers[52].

Abnormal activation of the Rho/ROCK pathway has been observed in various disorders of the central nervous system.

Injury to the adult vertebrate brain and spinal cord activates ROCKs, thereby inhibiting neurite growth and sprouting.

Inhibition of ROCKs results in accelerated regeneration and enhanced functional recovery after spinal-cord injury in mammals, and inhibition of the Rho/ROCK pathway has also proved to be efficacious in animal models of stroke, inflammatory and demyelinating diseases, Alzheimer's disease and neuropathic pain. ROCK inhibitors, therefore, have the potential for preventing neurodegeneration and stimulating neuroregeneration in various neurological disorders.

The role of the Rho/ROCK signaling pathway in inhibiting axonal regeneration in the central nervous system[53]

The Rho/Rho-associated coiled-coil containing protein kinase (Rho/ROCK) pathway is a major signaling pathway in the central nervous system, transducing inhibitory signals to block regeneration. After central nervous system damage, the main cause of impaired regeneration is the presence of factors that strongly inhibit regeneration in the surrounding microenvironment.


EMPRIN/CD147 is a target for COVID-19 treatment. EMPRIN literally means Aspirin. White willow bark is essentially aspirin. There have been studies showing the protective effect of Aspirin, or white willow, on COVID-19 Patients. The EMPRIN (CD147 gene) is a receptor for oligomannosidic glycans which require Mannose, N-Acetyl Glucosamine (NAG), and Fucose (Bladderwrack).

CD147 acts as the main upstream stimulator of matrix metalloproteinases (MMPs) which degrade myelin proteins. Genistein (Nattokinase), Myricetin (Sea buckthorn), Resveratrol, Betulinic acid (Prunella vulgaris), Oleanolic acid (Prunella vulgaris), and Glycyrrhetinic acid (Licorice) target specific MMPs. While Licorice and Skullcap helps to address the MAG gene associated with sialic acid, which “hides mannose.”

The Morning Prayer gene MATINS (MYH9 Gene) regulates EMPRIN/CD147. MATINS is associated with kinetic energy transduction. Artemisinin targets The Morning Prayer (MYH9) gene.

Lastly, all these networks seem to converge upon the ROCK. So basically, ROCK inhibition impacts the MAG gene associated with myelin and the Morning Prayer gene (The MATINS gene/MYH9), which ultimately impacts the function of EMPRIN/CD147, and subs